猪和重组胰岛素对糖原活性的计算机分析

{"title":"猪和重组胰岛素对糖原活性的计算机分析","authors":"","doi":"10.33263/proceedings21.045045","DOIUrl":null,"url":null,"abstract":"The study focuses on the anti-diabetic activity by molecular simulation of Recombinant Insulin, Porcine Insulin, and Glycogen. The sequence of these three molecules was retrieved, and 3D structures were modeled. A total of two different molecular simulations were carried out. The simulations were done using Autodock software. Initially, the downloaded PDB structures were docked with glycogen and the second between the active site peptide models of both insulin molecules based on castP prediction with glycogen molecule. The results were analyzed by the Ramachandran plot for model prediction, and the binding energy was set as criteria to determine the best-docked model. The binding energy of recombinant insulin, porcine insulin with glycogen was 0.32 and -1.09, respectively. Similarly, the binding energy for peptide models with a glycogen molecule was found to be +1.09 and +6.76, respectively. Based on the results, it was concluded that recombinant insulin has a higher affinity than porcine insulin.","PeriodicalId":90703,"journal":{"name":"Proceedings. International Meshing Roundtable","volume":"55 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2020-07-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"In-silico Analysis of Porcine and Recombinant Insulin Activity on Glycogen\",\"authors\":\"\",\"doi\":\"10.33263/proceedings21.045045\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The study focuses on the anti-diabetic activity by molecular simulation of Recombinant Insulin, Porcine Insulin, and Glycogen. The sequence of these three molecules was retrieved, and 3D structures were modeled. A total of two different molecular simulations were carried out. The simulations were done using Autodock software. Initially, the downloaded PDB structures were docked with glycogen and the second between the active site peptide models of both insulin molecules based on castP prediction with glycogen molecule. The results were analyzed by the Ramachandran plot for model prediction, and the binding energy was set as criteria to determine the best-docked model. The binding energy of recombinant insulin, porcine insulin with glycogen was 0.32 and -1.09, respectively. Similarly, the binding energy for peptide models with a glycogen molecule was found to be +1.09 and +6.76, respectively. Based on the results, it was concluded that recombinant insulin has a higher affinity than porcine insulin.\",\"PeriodicalId\":90703,\"journal\":{\"name\":\"Proceedings. International Meshing Roundtable\",\"volume\":\"55 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2020-07-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Proceedings. International Meshing Roundtable\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.33263/proceedings21.045045\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Proceedings. International Meshing Roundtable","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.33263/proceedings21.045045","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

摘要

通过分子模拟研究了重组胰岛素、猪胰岛素和糖原的抗糖尿病活性。检索了这三个分子的序列,并建立了三维结构模型。总共进行了两种不同的分子模拟。模拟使用Autodock软件完成。首先,下载的PDB结构与糖原对接,然后基于糖原分子的castP预测,在两个胰岛素分子的活性位点肽模型之间进行对接。采用Ramachandran图对模型预测结果进行分析,并以结合能为标准确定最佳对接模型。重组胰岛素和猪胰岛素与糖原的结合能分别为0.32和-1.09。同样,糖原分子多肽模型的结合能分别为+1.09和+6.76。结果表明,重组胰岛素具有比猪胰岛素更高的亲和力。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
In-silico Analysis of Porcine and Recombinant Insulin Activity on Glycogen
The study focuses on the anti-diabetic activity by molecular simulation of Recombinant Insulin, Porcine Insulin, and Glycogen. The sequence of these three molecules was retrieved, and 3D structures were modeled. A total of two different molecular simulations were carried out. The simulations were done using Autodock software. Initially, the downloaded PDB structures were docked with glycogen and the second between the active site peptide models of both insulin molecules based on castP prediction with glycogen molecule. The results were analyzed by the Ramachandran plot for model prediction, and the binding energy was set as criteria to determine the best-docked model. The binding energy of recombinant insulin, porcine insulin with glycogen was 0.32 and -1.09, respectively. Similarly, the binding energy for peptide models with a glycogen molecule was found to be +1.09 and +6.76, respectively. Based on the results, it was concluded that recombinant insulin has a higher affinity than porcine insulin.
求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
Controlling Intermolecular H-atom Abstraction with Ultrafast Pump-Push-Probe Spectroscopy New nanotechnologies for Energy saving and Resiliency of the Built Environment COVID-19 Global Healthcare System Failures: The Desperate Need for a Paradigm Shift for Better Medical Materials Piezoelectric on Natural Fiber Reinforced Epoxy Composite for Wireless Energy Harvesting Theoretical Investigation of Thermal Expansion Coefficients of SiC Reinforced Copper Matrix Composites
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1